Glucose-1-phosphate thymidylyltransferase

spinqualitylabelsall models Structure of glucose-1-phosphate thymidylyltransferase complex with TTP (PDB code 1g2v). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Glucose-1-phosphate thymidylyltransferase (RmlA) catalyzes the conversion of dTTP and α-D-glucose 1-phosphate (DGP) to diphosphate and dTDP-glucose or dTDP- rhamnose. RmlA participates in nucleotide sugars metabolism, streptomycin biosynthesis and polyketide sugar metabolism. Relevance dTDP- rhamnose is a component of bacterial cell wall, hence RmlA inhibition is a potential therapeutic target as drugs against pathogenic bacteria. Structural highlights RmlA 3D structure can be divided into three functional domains: a core domain which binds nucleotide, sugar-binding domain and dimerization domain. The active site is formed by the core and sugar-binding domains and the residues comprising it can be divided to catalytic residues (in cyan) and thymidine-specific residues (in green). A second TTP-binding site is seen in the structure. 3D structures of glucose-1-phosphate thymidylyltransferase Glucose-1-phosphate thymidylyltransferase 3D structures

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